Several different carbohydrate-free peptides have been obtained from cell walls of Staphylococcus aureus and Arthrobacter crystallopoietes by degradation with lytic enzymes. They all contained one residue ... [more ▼]

Several different carbohydrate-free peptides have been obtained from cell walls of Staphylococcus aureus and Arthrobacter crystallopoietes by degradation with lytic enzymes. They all contained one residue of amide ammonia per repeating subunit. A peptide obtained from cell walls of Micrococcus lysodeikticus contained no ammonia but had a glycine residue with a free carboxyl group. It has been demonstrated by Edman degradation that both the amide ammonia in the former two cell walls and the COOH-terminal glycine in the latter are substituted on the α-carboxyl group of glutamic acid. Other features of the structures of these peptides are discussed. [less ▲]

A teichoic acid-glycopeptide complex has been obtained from the cell wall of Staphylococcus aureus after enzymatic lysis of the walls with either of two acetylmuramidases. This complex was fractionated ... [more ▼]

A teichoic acid-glycopeptide complex has been obtained from the cell wall of Staphylococcus aureus after enzymatic lysis of the walls with either of two acetylmuramidases. This complex was fractionated into materials containing a glycopeptide component of varying size linked to teichoic acid. Most of the glycopeptide was removed by hydrolysis of the complexes with an acetylmuramyl-L-alanine amidase. After this treatment, a native teichoic acid with a weight-average molecular weight of about 20,000 and a number-average molecular weight of 12,000-16,000 was obtained. These data suggest that the largest molecules of the teichoic acid contain forty to fifty repeating units and that some smaller molecules also exist in the preparation. Chemical and physical analyses of native teichoic acid and various teichoic acid-glycopeptide complexes are presented. [less ▲]

Two disaccharides have previously been obtained in high yield from the cell wall of S. aureus by the use of hydrolytic enzymes. Disaccharide 1 is N-acetylglucosaminyl-N-acetylmuramic acid and disaccharide ... [more ▼]

Two disaccharides have previously been obtained in high yield from the cell wall of S. aureus by the use of hydrolytic enzymes. Disaccharide 1 is N-acetylglucosaminyl-N-acetylmuramic acid and disaccharide 2 is N-acetylglucosaminyl-N,Ogr;-diacetylmuramic acid. After hydrolysis of disaccharide 2 with Î²-acetylglucosaminidase, N,O-diacetylmuramic acid was prepd. Data obtained from periodate oxidn. of these compds. coupled with their susceptibility to Î²-acetylglucosaminidase indicate that both disaccharides are Î²-1,4-linked and that the O-acetyl group of disaccharide 2 is on the 6-position of N-acetylmuramic acid. The high reducing power and pos. Morgan-Elson reaction of the disaccharides are due to their unusual susceptibility to hydrolysis at alk. pH. These and other anomalous properties of the compds. are discussed. [on SciFinder(R)] [less ▲]

The staphylolytic enzyme recently isolated from cultures of a Chalaropsis species by Hash is shown to be an acetylmurainidase that cleaves all the glycosidic linkages of N-acetylmuramic acid and N,O ... [more ▼]

The staphylolytic enzyme recently isolated from cultures of a Chalaropsis species by Hash is shown to be an acetylmurainidase that cleaves all the glycosidic linkages of N-acetylmuramic acid and N,O-diacetylmuramic acid in the cell wall of Staphylococcus aureus strain Copenhagen. It is similar in specificity to the "32 enzyme" from Streptomyces albus but it differs from egg-white lysozyme whose activity is inhibited by the presence of O-acetyl groups. [less ▲]

The disaccharides, β-1,6-N-acetylglucosamimyl-N-acetylmuramic acid and β-1,6-N-acetyl-glucosaminyl-N,4-O-diacetylmuramic acid, have been identified as products of hydrolysis of the cell wall of S. aureus ... [more ▼]

The disaccharides, β-1,6-N-acetylglucosamimyl-N-acetylmuramic acid and β-1,6-N-acetyl-glucosaminyl-N,4-O-diacetylmuramic acid, have been identified as products of hydrolysis of the cell wall of S. aureus by an acetylmuramidase and an amidase from Streptomyces albus G. N-acetylmuramic acid and N,4-O-diacetylmuramic acid were formed from these compounds after hydrolysis with a β-acetylglucosarninidase. The data obtained do not exclude the presence of a small percentage of disaccharides with other linkages, however. Several bases for the resistance of cell walls of S. aureus to hydrolysis by egg white lysozyme have been discussed. [less ▲]

The cell wall of S. aureus strain Copenhagen, has been solubilized through the action of the 32 enzyme" isolated from Streptomyces albus G. This solubilization was the consequence of hydrolysis of ... [more ▼]

The cell wall of S. aureus strain Copenhagen, has been solubilized through the action of the 32 enzyme" isolated from Streptomyces albus G. This solubilization was the consequence of hydrolysis of acetylamino sugar linkages in the cell wall [less ▲]